ID A0A2H5Q3B0_CITUN Unreviewed; 1064 AA.
AC A0A2H5Q3B0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN ORFNames=CUMW_191790 {ECO:0000313|EMBL:GAY59071.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY59071.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY59071.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00048694};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY59071.1}.
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DR EMBL; BDQV01000202; GAY59071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5Q3B0; -.
DR STRING; 55188.A0A2H5Q3B0; -.
DR Proteomes; UP000236630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR FunFam; 3.40.1110.10:FF:000021; calcium-transporting ATPase, endoplasmic reticulum-type; 1.
DR FunFam; 2.70.150.10:FF:000014; Calcium-transporting ATPase, putative; 1.
DR FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 1.
DR FunFam; 1.20.1110.10:FF:000077; ECA1 (ER-TYPE CA2+-ATPASE 1); 1.
DR FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000236630};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1007
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..101
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1064 AA; 117162 MW; 0191811C9F547230 CRC64;
MGKGGEDYGL RKVISEAKTS EDREIFPAWA KSVDECEKHY GVRKRFGLKS AEVERRRKIY
GLNELEKHEG PSIWSLILEQ FNDTLVRILL GAAVISFVLA WYDGEEGGEK EITAFVEPLV
IFMILILNAI VGVWQENNAE KALEALKEIQ SEHAAVIRDG SKIPKLPAKE LVPGDIVELK
VGDRVPADMR VVELISSTLR VEQGSLTGES EAVNKTNKIV PLDTDMQGKK CMLFAGTTIV
NGNCVCLVTQ IGMETEIGKV HNQIYVASQS EEDTPLKKKL NDFGEVLTKM IGIICVFVWL
INLKYFLSWQ NVDGWPRNFK FSFEKCTYYL KIAVALAVAA IPEGLPAVIT TCLALGTRKM
AQKNALVRKL PSVETLGCTT VICSDKTGTL TTNQMAVAKL VAVGGGVDKL RSFNVDGTTY
SPYDGKIHDW TPGRLDANLQ MIAKIAAVCN DAGIVHSENK YVSHGMPTEA ALKVLVEKMG
LPEGSRDYES RIGDEILSCC RMWNEYERRI ATLEFDRDRK SMGVIVNSQL GKRSLFVKGA
VENVLERSTK MQLLDGSVVP VDHKSRNLIL DALHEMSTGA LRCLGFAYKD KLPDFETYDG
NEDHPAHTLL LNPSNYASIE CGLTFVGLVG LRDPPRNEVH QAIEDCRAAG IRVMVITGDN
KNTAEAICRE IGVFECNEDI SLKSLTGKEF MEMHDKKAHL RQSGGLLFSR AEPRHKQEIV
RLLKEDGEVV AMTGDGVNDA PALKLADIGI AMGIAGTEVA KEASDMVLAD DDFSTIVSAV
GEGRSIYNNM KAFIRYMISS NIGEVASIFF TAALGIPEGL IPVQLLWVNL VTDGPPATAL
GFNPPDKDIM KKPPRRSDDS LISAWILFRY LVIGLYVGIA TVGVFIIWYT HGSFLGINLI
GDGHSLVTYS QLTNWGQCPS WGNFTVSPFT AGNQVFTFND NPCDYFHGGK VKAMTLSLSV
LVAIEMFNSL NALSEDGSLL TMPPWVNPWL LLAMSVSFGL HFLILYVPFL AQIFGIVPLS
FNEWLLVLAI AFPVVLIDEV LKFVGRCTNG SQTSRRKSSK PKSE
//
